{"doi":"10.1002/pep2.24274","title":"Issue Information","abstract":"Nuclear magnetic resonance (NMR) spectroscopy is a versatile method for studying folding in peptides, proteins, and their mimetics.In natural entities, the straightforward to obtain metric of proton chemical shift provides residue-level insights into folded structure as well as dynamics.Rao et al. report the expansion of such methods to protein-like chains with non-canonical backbone compositions.Comparison of the NMR properties of a library of artificial residues in random coil and helical contexts reveals systematic chemical shift changes associated with certain residues adopting a helical folded conformation.","journal":"Peptide Science","year":2023,"id":403957,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9442,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2023-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[],"reference_count":0,"raw_metadata":null,"created_at":"2026-07-19T01:20:40.264741Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}